ID   A0A022MNQ2_9ACTN        Unreviewed;       476 AA.
AC   A0A022MNQ2;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=Glutamate decarboxylase {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
DE            EC=4.1.1.15 {ECO:0000256|ARBA:ARBA00012421, ECO:0000256|RuleBase:RU361171};
GN   ORFNames=CF54_09975 {ECO:0000313|EMBL:EYT82998.1};
OS   Streptomyces sp. Tu 6176.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1470557 {ECO:0000313|EMBL:EYT82998.1, ECO:0000313|Proteomes:UP000020060};
RN   [1] {ECO:0000313|EMBL:EYT82998.1, ECO:0000313|Proteomes:UP000020060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu 6176 {ECO:0000313|EMBL:EYT82998.1,
RC   ECO:0000313|Proteomes:UP000020060};
RA   Olano C., Cano-Prieto C., Mendez C., Salas J.A.;
RT   "Draft genome sequence of Streptomyces sp. Tu 6176, producer of the
RT   cytotoxic benzoxazol nataxazol.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2;
CC         Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15;
CC         Evidence={ECO:0000256|ARBA:ARBA00000018,
CC         ECO:0000256|RuleBase:RU361171};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|RuleBase:RU000382}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EYT82998.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JFJQ01000299; EYT82998.1; -; Genomic_DNA.
DR   RefSeq; WP_037889583.1; NZ_KK106988.1.
DR   AlphaFoldDB; A0A022MNQ2; -.
DR   HOGENOM; CLU_019582_2_1_11; -.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000020060; Unassembled WGS sequence.
DR   GO; GO:0004351; F:glutamate decarboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   GO; GO:0006536; P:glutamate metabolic process; IEA:InterPro.
DR   CDD; cd06450; DOPA_deC_like; 1.
DR   Gene3D; 3.90.1150.160; -; 1.
DR   Gene3D; 4.10.280.50; -; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010107; Glutamate_decarboxylase.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   NCBIfam; TIGR01788; Glu-decarb-GAD; 1.
DR   PANTHER; PTHR43321; GLUTAMATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR43321:SF3; GLUTAMATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Decarboxylase {ECO:0000256|RuleBase:RU361171};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   REGION          447..476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   476 AA;  53337 MW;  3898731F893F538D CRC64;
     MTVRHSRDDR GDSRDLAVNP VFSREPLQVP RYALPRAEMD PDTAYQIVHD ELMLDGNARQ
     NLATFVSTWA EPQARRLMDE CAEKNMIDKD EYPQTAEVET RCVHMLARLW HAEDPRRAVG
     CSTTGSSEAA MLGGLALKRR WQHRRRAEGK PADRPNLVMG INVQICWEKF ADYFEVEPRY
     VPMEGDRYHL TPEQAVELCD ENTIGVVAVL GSTFDGSYEP VAAIAAALDD LQERTGLDIP
     VHVDGASGGM IAPFLDPDLE WDFRLPRVAS INTSGHKYGL VMPGVGWALW RDKTALPDDL
     VFHVNYLGGD MPTFALNFSR PGAQVVAQYY NFLRLGFEGY RRVQQTCRDV ATRLAAEIAR
     LGPFELITDG SEIPVFAFRM SEGTDHFSVF DVSAALRESG WLVPAYTFPK NRTDLAVLRI
     VVRNGFSHDL ADLLLADLRR VLPRLDKQNE PHRTADDAGG FAHGAETKNP RSPGRD
//